ID   MEP2_ASPFN              Reviewed;         639 AA.
AC   B8NMK3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Extracellular metalloproteinase mep;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase mep;
DE   AltName: Full=Fungalysin mep;
DE   Flags: Precursor;
GN   Name=mep; ORFNames=AFLA_124390;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; EQ963481; EED48216.1; -; Genomic_DNA.
DR   RefSeq; XP_002381632.1; XM_002381591.1.
DR   AlphaFoldDB; B8NMK3; -.
DR   SMR; B8NMK3; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EED48216; EED48216; AFLA_124390.
DR   VEuPathDB; FungiDB:AFLA_124390; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; IRKDSYT; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   PRINTS; PR00999; FUNGALYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..245
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407160"
FT   CHAIN           246..639
FT                   /note="Extracellular metalloproteinase mep"
FT                   /id="PRO_0000407161"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        368
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  70855 MW;  2D15916567DF1D15 CRC64;
     MHMLSFIGAL ALPVFVCAQS CEPASLSPRL AGVDLEKFRL TPNAEYVDSD QQIPISTTNV
     GLIEQSYVET AIKLVRETFP TASFRLREDH YVGDNGVAHV HFRQTVHDLD VDNGDFNVNV
     GRDGSVFSYG NSFYTGPVPS ITQLTKRDFT DPVAALKFAL THLQLPITAG DVSAESTEHP
     HKYILRGTSG AVTDPKARLV YLVKPEGTLC LVWRVETDVD DNWLLTYVDA KTAEDIHGVV
     DYISEATFQV YGWGINDPGQ VDSRAVLTDP WNLKESPLTW FSDGQKNWTT TRGNNGIAQE
     NINNLPTYLN NFRPDSPTQN FSYEYPAGGS PKDYINASIT QLFYTANAYH DLLYTLGFNE
     KAGNFQWNNS GLGGKDKDYV ILNAQDGASR NNADFATPPD GSPARMRMYL FTHTTPPRDG
     VFESGIVIHE YTHGLSMRLT GGPDNSRCLS AFESASMGEG WGDFMATAIR LKPSDTRATD
     YGMGMWVYND EKGIRQYLYS TSMETNPLNY TSLNRMWEAH AGGTVWASML YEVLWNLIDK
     HGKNDGPRPT FDERGVPRDG KYLAMKIVID AMALQPCNPD FVQARNAILD ADQALTGGQN
     KCEIWTGFAK RGLGQGAEYG RGRRVGSYDI PSGVCQKKI